RSRC1_BOVIN
ID RSRC1_BOVIN Reviewed; 334 AA.
AC Q2T9Y0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Serine/Arginine-related protein 53;
DE Short=SRrp53;
DE AltName: Full=Arginine/serine-rich coiled-coil protein 1;
GN Name=RSRC1; Synonyms=SRRP53;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in pre-mRNA splicing. Involved both in the
CC constitutive and regulation of pre-mRNA splicing. May have a role in
CC the recognition of the 3' splice site during the second step of
CC splicing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via Arg/Ser-rich domain) with LUC7L3, RBM39 and
CC RSF1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the
CC nucleus and cytoplasm. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9DBU6}.
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DR EMBL; BC111215; AAI11216.1; -; mRNA.
DR RefSeq; NP_001068872.1; NM_001075404.1.
DR AlphaFoldDB; Q2T9Y0; -.
DR SMR; Q2T9Y0; -.
DR STRING; 9913.ENSBTAP00000042183; -.
DR PaxDb; Q2T9Y0; -.
DR PRIDE; Q2T9Y0; -.
DR Ensembl; ENSBTAT00000044707; ENSBTAP00000042183; ENSBTAG00000031561.
DR GeneID; 509437; -.
DR KEGG; bta:509437; -.
DR CTD; 51319; -.
DR VEuPathDB; HostDB:ENSBTAG00000031561; -.
DR VGNC; VGNC:53602; RSRC1.
DR eggNOG; KOG3406; Eukaryota.
DR GeneTree; ENSGT00730000111251; -.
DR HOGENOM; CLU_072086_0_0_1; -.
DR InParanoid; Q2T9Y0; -.
DR OMA; VIFHPNF; -.
DR OrthoDB; 1367755at2759; -.
DR TreeFam; TF336021; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000031561; Expressed in semen and 106 other tissues.
DR ExpressionAtlas; Q2T9Y0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR InterPro; IPR034604; SRRP53.
DR PANTHER; PTHR31968; PTHR31968; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..334
FT /note="Serine/Arginine-related protein 53"
FT /id="PRO_0000401193"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..225
FT /evidence="ECO:0000255"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 38710 MW; 1C4E104CE410FC25 CRC64;
MGRRSSDTEE ESRSKRKKKH RRRSSSSSSS DSRTYSRKKG GRRSRSKSRS WSRDLQPRSH
SYDRRRRHRS SSSSSYGSRR KRSQSRSRGR GKSYRVQRSR SKSRTRRSRS RPRPRSHSRS
SERSSHRRTR SRSRDRERRK GRDKEKREKE KDKGKDKELH NIKRGESGNI KAGLEHLPPA
EQAKARLQLV LEAAAKADEA LKAKERNEEE AKRRKEEDQT TLVEQVKRVK EIEAIESDSF
VQQTFRSSKE IKKAVEASEV KHAATTSGPA SVVADPPSNE KEIDPSNIPT AIKYQDDNSL
AHPNLFIEKA DAEEKWFKRL IALRQERLMG SPVA